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J. Biol. Chem., Vol. 276, Issue 23, 20286-20291, June 8, 2001
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From the § Department of Chemistry, University of
Minnesota, Minneapolis, Minnesota 55455, the ** Department of
Biochemistry and Molecular Pharmacology, Thomas Jefferson University,
Philadelphia, Pennsylvania 19107, and the Analysis of prolyl-tRNA synthetase (ProRS) across
all three taxonomic domains (Eubacteria, Eucarya, and Archaea) reveals
that the sequences are divided into two distinct groups. Recent studies show that Escherichia coli ProRS, a member of the
"prokaryotic-like" group, recognizes specific tRNA bases at both
the acceptor and anticodon ends, whereas human ProRS, a member of the
"eukaryotic-like" group, recognizes nucleotide bases primarily in
the anticodon. The archaeal Methanococcus jannaschii ProRS
is a member of the eukaryotic-like group, although its
tRNAPro possesses prokaryotic features in the acceptor
stem. We show here that, in some respects, recognition of
tRNAPro by M. jannaschii ProRS parallels that
of human, with a strong emphasis on the anticodon and only weak
recognition of the acceptor stem. However, our data also indicate
differences in the details of the anticodon recognition between these
two eukaryotic-like synthetases. Although the human enzyme places a
stronger emphasis on G35, the M. jannaschii enzyme places a
stronger emphasis on G36, a feature that is shared by E. coli ProRS. These results, interpreted in the context of an
extensive sequence alignment, provide evidence of divergent adaptation
by M. jannaschii ProRS; recognition of the tRNA acceptor
end is eukaryotic-like, whereas the details of the anticodon
recognition are prokaryotic-like. This divergence may be a reflection
of the unusual dual function of this enzyme, which catalyzes specific
aminoacylation with proline as well as with cysteine.
Divergent Adaptation of tRNA Recognition
by Methanococcus jannaschii Prolyl-tRNA Synthetase*
§¶,
**,, Department
of Cell Biology, Cancer Institute, Japanese Foundation for Cancer
Research, Kami-Ikebukuro, Toshima-Ku, Tokyo 170, Japan
*
This work was funded by National Institutes of Health Grants
GM49928 (to K. M.-F.) and GM56662 (to Y.-M. H.) and by a grant from
the Ministry of Education, Science, and Culture, Japan (to K. S.). In
addition, partial support of the research was provided by the National
Science Foundation (MCB-9904956 to Y.-M. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contribute equally to this work.
¶
Supported by a National Institutes of Health Molecular
Biophysics Training Grant.
Supported by the American Heart Association,
Pennsylvania-Delaware Affiliate.
§§
To whom correspondence may be addressed. Tel.: 612-624-0286;
Fax: 612-626-7541; E-mail: musier@chem.umn.edu.
¶¶
To whom correspondence may be addressed. Tel.:
215-503-4480; Fax: 215-923-9162; E-mail: Ya-Ming.Hou@mail.tju.edu.
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